Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phenylalanine-4-hydroxylase

Gene

phhA

Organism
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin.

Cofactori

Pathwayi: L-phenylalanine degradation

This protein is involved in step 1 of the subpathway that synthesizes acetoacetate and fumarate from L-phenylalanine.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Phenylalanine-4-hydroxylase (phhA)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. no protein annotated in this organism
  5. no protein annotated in this organism
  6. no protein annotated in this organism
This subpathway is part of the pathway L-phenylalanine degradation, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetoacetate and fumarate from L-phenylalanine, the pathway L-phenylalanine degradation and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi138Iron1
Metal bindingi143Iron1
Metal bindingi184Iron1

GO - Molecular functioni

  • iron ion binding Source: InterPro
  • phenylalanine 4-monooxygenase activity Source: CACAO

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Phenylalanine catabolism

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-12067.
BRENDAi1.14.16.1. 1370.
UniPathwayiUPA00139; UER00337.

Names & Taxonomyi

Protein namesi
Recommended name:
Phenylalanine-4-hydroxylase (EC:1.14.16.1)
Short name:
PAH
Alternative name(s):
Phe-4-monooxygenase
Gene namesi
Name:phhA
Ordered Locus Names:CV_3180
OrganismiChromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Taxonomic identifieri243365 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNeisserialesChromobacteriaceaeChromobacterium
Proteomesi
  • UP000001424 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002055531 – 297Phenylalanine-4-hydroxylaseAdd BLAST297

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

STRINGi243365.CV_3180.

Structurei

Secondary structure

1297
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi12 – 16Combined sources5
Turni17 – 19Combined sources3
Turni24 – 26Combined sources3
Helixi33 – 35Combined sources3
Helixi38 – 54Combined sources17
Turni56 – 58Combined sources3
Helixi61 – 69Combined sources9
Beta strandi74 – 76Combined sources3
Helixi80 – 91Combined sources12
Beta strandi94 – 101Combined sources8
Helixi104 – 112Combined sources9
Beta strandi115 – 119Combined sources5
Helixi125 – 127Combined sources3
Beta strandi128 – 130Combined sources3
Helixi136 – 143Combined sources8
Helixi145 – 148Combined sources4
Helixi150 – 161Combined sources12
Helixi163 – 168Combined sources6
Helixi172 – 181Combined sources10
Turni182 – 185Combined sources4
Beta strandi187 – 190Combined sources4
Beta strandi193 – 196Combined sources4
Helixi199 – 202Combined sources4
Helixi207 – 213Combined sources7
Beta strandi215 – 221Combined sources7
Helixi224 – 228Combined sources5
Beta strandi234 – 236Combined sources3
Beta strandi239 – 245Combined sources7
Helixi247 – 253Combined sources7
Helixi259 – 266Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LTUX-ray1.74A1-297[»]
1LTVX-ray2.00A1-297[»]
1LTZX-ray1.40A1-297[»]
3TCYX-ray1.55A1-297[»]
3TK2X-ray1.35A1-297[»]
3TK4X-ray1.50A1-297[»]
4ESMX-ray1.35A1-297[»]
4ETLX-ray1.49A1-297[»]
4JPXX-ray1.55A1-297[»]
4JPYX-ray2.13A1-297[»]
4Q3WX-ray1.40A1-297[»]
4Q3XX-ray1.35A1-297[»]
4Q3YX-ray1.40A1-297[»]
4Q3ZX-ray1.35A1-297[»]
ProteinModelPortaliP30967.
SMRiP30967.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30967.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105MIR. Bacteria.
COG3186. LUCA.
HOGENOMiHOG000253806.
KOiK00500.
OMAiHEVFGHC.
OrthoDBiPOG091H05UQ.

Family and domain databases

Gene3Di1.10.800.10. 1 hit.
InterProiIPR001273. ArAA_hydroxylase.
IPR018301. ArAA_hydroxylase_Fe/CU_BS.
IPR019774. Aromatic-AA_hydroxylase_C.
IPR005960. Phe-4-hydroxylase_mono.
[Graphical view]
PANTHERiPTHR11473. PTHR11473. 1 hit.
PfamiPF00351. Biopterin_H. 1 hit.
[Graphical view]
PRINTSiPR00372. FYWHYDRXLASE.
SUPFAMiSSF56534. SSF56534. 1 hit.
TIGRFAMsiTIGR01267. Phe4hydrox_mono. 1 hit.
PROSITEiPS00367. BH4_AAA_HYDROXYL_1. 1 hit.
PS51410. BH4_AAA_HYDROXYL_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P30967-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDRADFVVP DITTRKNVGL SHDANDFTLP QPLDRYSAED HATWATLYQR
60 70 80 90 100
QCKLLPGRAC DEFMEGLERL EVDADRVPDF NKLNQKLMAA TGWKIVAVPG
110 120 130 140 150
LIPDDVFFEH LANRRFPVTW WLREPHQLDY LQEPDVFHDL FGHVPLLINP
160 170 180 190 200
VFADYLEAYG KGGVKAKALG ALPMLARLYW YTVEFGLINT PAGMRIYGAG
210 220 230 240 250
ILSSKSESIY CLDSASPNRV GFDLMRIMNT RYRIDTFQKT YFVIDSFKQL
260 270 280 290
FDATAPDFAP LYLQLADAQP WGAGDVAPDD LVLNAGDRQG WADTEDV
Length:297
Mass (Da):33,616
Last modified:October 24, 2003 - v4
Checksum:i6D29A04203E906FD
GO

Sequence cautioni

The sequence AAA23115 differs from that shown. Reason: Frameshift at position 172.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti64M → L (PubMed:1655752).Curated1
Sequence conflicti64M → L (Ref. 2) Curated1
Sequence conflicti85Q → E (PubMed:1655752).Curated1
Sequence conflicti85Q → E (Ref. 2) Curated1
Sequence conflicti276V → I (PubMed:1655752).Curated1
Sequence conflicti276V → I (Ref. 2) Curated1
Sequence conflicti288R → H (PubMed:1655752).Curated1
Sequence conflicti288R → H (Ref. 2) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55915 Genomic DNA. Translation: AAA23115.1. Frameshift.
AF146711 Genomic DNA. Translation: AAD37774.1.
AE016825 Genomic DNA. Translation: AAQ60846.1.
PIRiA40996.

Genome annotation databases

EnsemblBacteriaiAAQ60846; AAQ60846; CV_3180.
KEGGicvi:CV_3180.
PATRICi21441114. VBIChrVio67196_3099.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55915 Genomic DNA. Translation: AAA23115.1. Frameshift.
AF146711 Genomic DNA. Translation: AAD37774.1.
AE016825 Genomic DNA. Translation: AAQ60846.1.
PIRiA40996.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LTUX-ray1.74A1-297[»]
1LTVX-ray2.00A1-297[»]
1LTZX-ray1.40A1-297[»]
3TCYX-ray1.55A1-297[»]
3TK2X-ray1.35A1-297[»]
3TK4X-ray1.50A1-297[»]
4ESMX-ray1.35A1-297[»]
4ETLX-ray1.49A1-297[»]
4JPXX-ray1.55A1-297[»]
4JPYX-ray2.13A1-297[»]
4Q3WX-ray1.40A1-297[»]
4Q3XX-ray1.35A1-297[»]
4Q3YX-ray1.40A1-297[»]
4Q3ZX-ray1.35A1-297[»]
ProteinModelPortaliP30967.
SMRiP30967.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243365.CV_3180.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAQ60846; AAQ60846; CV_3180.
KEGGicvi:CV_3180.
PATRICi21441114. VBIChrVio67196_3099.

Phylogenomic databases

eggNOGiENOG4105MIR. Bacteria.
COG3186. LUCA.
HOGENOMiHOG000253806.
KOiK00500.
OMAiHEVFGHC.
OrthoDBiPOG091H05UQ.

Enzyme and pathway databases

UniPathwayiUPA00139; UER00337.
BioCyciMetaCyc:MONOMER-12067.
BRENDAi1.14.16.1. 1370.

Miscellaneous databases

EvolutionaryTraceiP30967.

Family and domain databases

Gene3Di1.10.800.10. 1 hit.
InterProiIPR001273. ArAA_hydroxylase.
IPR018301. ArAA_hydroxylase_Fe/CU_BS.
IPR019774. Aromatic-AA_hydroxylase_C.
IPR005960. Phe-4-hydroxylase_mono.
[Graphical view]
PANTHERiPTHR11473. PTHR11473. 1 hit.
PfamiPF00351. Biopterin_H. 1 hit.
[Graphical view]
PRINTSiPR00372. FYWHYDRXLASE.
SUPFAMiSSF56534. SSF56534. 1 hit.
TIGRFAMsiTIGR01267. Phe4hydrox_mono. 1 hit.
PROSITEiPS00367. BH4_AAA_HYDROXYL_1. 1 hit.
PS51410. BH4_AAA_HYDROXYL_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPH4H_CHRVO
AccessioniPrimary (citable) accession number: P30967
Secondary accession number(s): Q9R634, Q9XC88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 24, 2003
Last modified: November 2, 2016
This is version 145 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.